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VNNL3_DROME
ID   VNNL3_DROME             Reviewed;         523 AA.
AC   P83548; D8FT28;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Vanin-like protein 3 {ECO:0000312|FlyBase:FBgn0052750};
DE            EC=3.5.1.- {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=CG32750 {ECO:0000312|FlyBase:FBgn0052750};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000312|EMBL:AAF46129.2};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000305}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3] {ECO:0000312|EMBL:ADJ93823.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=25387828; DOI=10.1534/g3.114.015040;
RA   Logan-Garbisch T., Bortolazzo A., Luu P., Ford A., Do D., Khodabakhshi P.,
RA   French R.L.;
RT   "Developmental ethanol exposure leads to dysregulation of lipid metabolism
RT   and oxidative stress in Drosophila.";
RL   G3 (Bethesda) 5:49-59(2014).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC       anchor {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in third instar larvae.
CC       {ECO:0000269|PubMed:25387828}.
CC   -!- INDUCTION: Induced by ethanol. {ECO:0000269|PubMed:25387828}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       BTD/VNN family. {ECO:0000305}.
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DR   EMBL; AE014298; AAF46129.2; -; Genomic_DNA.
DR   EMBL; BT125050; ADJ93823.1; -; mRNA.
DR   RefSeq; NP_727067.1; NM_167060.3.
DR   AlphaFoldDB; P83548; -.
DR   SMR; P83548; -.
DR   STRING; 7227.FBpp0070846; -.
DR   GlyGen; P83548; 5 sites.
DR   PaxDb; P83548; -.
DR   EnsemblMetazoa; FBtr0070881; FBpp0070846; FBgn0052750.
DR   GeneID; 326238; -.
DR   KEGG; dme:Dmel_CG32750; -.
DR   UCSC; CG32750-RA; d. melanogaster.
DR   FlyBase; FBgn0052750; CG32750.
DR   VEuPathDB; VectorBase:FBgn0052750; -.
DR   eggNOG; KOG0806; Eukaryota.
DR   GeneTree; ENSGT00390000013823; -.
DR   HOGENOM; CLU_033209_1_0_1; -.
DR   InParanoid; P83548; -.
DR   OMA; ADLCCDF; -.
DR   OrthoDB; 1276751at2759; -.
DR   PhylomeDB; P83548; -.
DR   BioGRID-ORCS; 326238; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 326238; -.
DR   PRO; PR:P83548; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0052750; Expressed in adult Malpighian tubule (Drosophila) and 9 other tissues.
DR   Genevisible; P83548; DM.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd07567; biotinidase_like; 1.
DR   Gene3D; 3.60.110.10; -; 1.
DR   InterPro; IPR012101; Biotinidase-like_euk.
DR   InterPro; IPR040154; Biotinidase/VNN.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR043957; Vanin_C.
DR   PANTHER; PTHR10609; PTHR10609; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   Pfam; PF19018; Vanin_C; 1.
DR   PIRSF; PIRSF011861; Biotinidase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW   Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..498
FT                   /note="Vanin-like protein 3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000019726"
FT   PROPEP          499..523
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000450615"
FT   DOMAIN          29..298
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        74
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        167
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        200
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   LIPID           498
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        468
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   523 AA;  59133 MW;  BA1588AD6750EB9F CRC64;
     MAVFLRRFLW LISFTLVLTD DNSVENKFYI AGVVEYRPTF MGGTSEQLLQ ANLAGYLEIM
     ASGNGTTDII VFPEATLNSV ITLTAVPKFT EQSLCEEQGD DDPEIAPFLR SLACAAREYG
     TYLVVNVKER VSEQCTSDET CSSRGYSIHN TNVVFDRQGA VISRYRKWNL YLEPSTNRTE
     SPEIATFTTD FNVTFGHFIC FDMLFYTPAQ DLVEQLGIRH VIVTKMFNSE LPFLTASQFQ
     QGWAWANRVN LLASGGSLPQ GGISGSGIYA GQQGALARLM ITDELVGQRK LLLAKVPLDP
     EEPIATDEIL EPEIMTPVKL KLLQQPELKN FTTWELPMVR GSSVDKRICQ EDLCCEFRVT
     WTLEDTQPEY NYRLGVWVGQ RRYEEEQYSA IRLCGLFACK GASVESCGLV SEEEVHLQDH
     RVVFTDLQIL GEFVRRPRRL ILPSTLSSSS FYALQPSQLA WSMEELANVT RIKMELRQPH
     SQLMTFAIYG NYFDEYANGG AGRLGTLLFL LITPLIMMHL FRE
 
 
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